P53_XENLA
ID P53_XENLA Reviewed; 363 AA.
AC P07193;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cellular tumor antigen p53;
DE AltName: Full=Tumor suppressor p53;
GN Name=tp53;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2830576;
RA Soussi T., de Fromentel C.C., Mechali M., May P., Kress M.;
RT "Cloning and characterization of a cDNA from Xenopus laevis coding for a
RT protein homologous to human and murine p53.";
RL Oncogene 1:71-78(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8302570;
RA Hoever M., Clement J.H., Wedlich D., Montenarh M., Knoechel W.;
RT "Overexpression of wild-type p53 interferes with normal development in
RT Xenopus laevis embryos.";
RL Oncogene 9:109-120(1994).
CC -!- FUNCTION: Acts as a tumor suppressor in many tumor types; induces
CC growth arrest or apoptosis depending on the physiological circumstances
CC and cell type. Involved in cell cycle regulation as a trans-activator
CC that acts to negatively regulate cell division by controlling a set of
CC genes required for this process. One of the activated genes is an
CC inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be
CC mediated either by stimulation of BAX and FAS antigen expression, or by
CC repression of Bcl-2 expression (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Binds DNA as a homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; M36962; AAA49923.1; -; mRNA.
DR EMBL; X05191; CAA28821.1; -; mRNA.
DR EMBL; X77546; CAA54672.1; -; mRNA.
DR EMBL; S68353; AAC60746.1; -; mRNA.
DR PIR; A29376; A29376.
DR RefSeq; NP_001081567.1; NM_001088098.1.
DR AlphaFoldDB; P07193; -.
DR SMR; P07193; -.
DR BioGRID; 99262; 1.
DR IntAct; P07193; 1.
DR TCDB; 1.C.110.1.2; the pore-forming pnc-27 peptide of 32 aas from the p53 tumor suppressor protein (pnc-27) family.
DR iPTMnet; P07193; -.
DR DNASU; 397926; -.
DR GeneID; 397926; -.
DR KEGG; xla:397926; -.
DR CTD; 397926; -.
DR Xenbase; XB-GENE-6252168; tp53.L.
DR OrthoDB; 257530at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397926; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd08367; P53; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR013872; p53_transactivation_domain.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF08563; P53_TAD; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Activator; Apoptosis; Cell cycle; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Zinc.
FT CHAIN 1..363
FT /note="Cellular tumor antigen p53"
FT /id="PRO_0000185726"
FT DNA_BIND 76..267
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Transcription activation (acidic)"
FT REGION 248..255
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 257..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..331
FT /note="Oligomerization"
FT REGION 344..356
FT /note="Basic (repression of DNA-binding)"
FT MOTIF 275..292
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 314..325
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 257..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 94
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="T -> S (in Ref. 2; CAA54672)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Missing (in Ref. 2; CAA54672)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Missing (in Ref. 2; CAA54672/AAC60746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40693 MW; CE1F3E58F020D74D CRC64;
MEPSSETGMD PPLSQETFED LWSLLPDPLQ TVTCRLDNLS EFPDYPLAAD MTVLQEGLMG
NAVPTVTSCA VPSTDDYAGK YGLQLDFQQN GTAKSVTCTY SPELNKLFCQ LAKTCPLLVR
VESPPPRGSI LRATAVYKKS EHVAEVVKRC PHHERSVEPG EDAAPPSHLM RVEGNLQAYY
MEDVNSGRHS VCVPYEGPQV GTECTTVLYN YMCNSSCMGG MNRRPILTII TLETPQGLLL
GRRCFEVRVC ACPGRDRRTE EDNYTKKRGL KPSGKRELAH PPSSEPPLPK KRLVVVDDDE
EIFTLRIKGR SRYEMIKKLN DALELQESLD QQKVTIKCRK CRDEIKPKKG KKLLVKDEQP
DSE
